Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 413, Issue 1, Pages 58-61Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2011.08.043
Keywords
DPF2; Cys2His2 type zinc finger; Crystal structure; d4-Protein family
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Funding
- Canadian Institutes for Health Research [1097737]
- Canadian Foundation for Innovation
- Genome Canada through the Ontario Genomics Institute
- GlaxoSmithKline
- Karolinska Institutet
- Knut and Alice Wallenberg Foundation
- Ontario Innovation Trust
- Ontario Ministry for Research and Innovation
- Merck Co., Inc.
- Novartis Research Foundation
- Swedish Agency for Innovation Systems
- Swedish Foundation for Strategic Research
- Wellcome Trust
- National Science Foundation of China [30670429]
- Natural Science Foundation of Hubei Province of China [2010CDB01206]
- Department of Energy, Office of Biological and Environmental Research [DE-AC02-06CH11357]
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DPF2 is an evolutionary highly conserved member of the d4-protein family characterized by an N-terminal 2/3 domain, a C2H2-type zinc finger (ZF), and a C-terminal tandem PHD zinc finger. DPF2 is identified as a transcription factor and may be related with some cancers in human. Here, we report the crystal structure of the C2H2-type zinc finger domain of human DPF2 with a canonical C2H2 fold, which contains two beta strands and one alpha helix. Several conserved residues, including Lys207, Lys216 and Arg217, constitute a positively charged surface in C2H2 domain, which implicates that it has the potential to bind DNA. The side chains of the residues Y209, C211, C214, 1(216, Y218, 1224, H227 and H232 form the hydrophobic core of C2H2 domain, which indicates a potential-binding surface in the human DPF2. (C) 2011 Elsevier Inc. All rights reserved.
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